Evidence map›Paper›PMID 32374871›Full record

ArticleNucleic acids research2020

DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs.

Adriana Roithová, Zuzana Feketová, Štěpánka Vaňáčová, David Staněk

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  7. Sm complex assembly and 5' cap trimethylation promote selective processing of snRNAs by the 3' exonuclease TOE1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. A shape-shifting nuclease unravels structured RNA.Nature structural & molecular biology · 2023
    Article
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  11. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Adriana RoithováLaboratory of RNA Biology, Institute of Molecular Genetics of the Czech Academy of Sciences, Videnska 1083, 14220 Prague, Czech Republic.
Zuzana FeketováCEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5/A35, 625 00 Brno, Czech Republic.
Štěpánka VaňáčováCEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5/A35, 625 00 Brno, Czech Republic.
David StaněkLaboratory of RNA Biology, Institute of Molecular Genetics of the Czech Academy of Sciences, Videnska 1083, 14220 Prague, Czech Republic.
Central European Institute of Technology · CZCzech Academy of Sciences · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spliceosomal small nuclear ribonucleoprotein particles (snRNPs) undergo a complex maturation pathway containing multiple steps in the nucleus and in the cytoplasm. snRNP biogenesis is strictly proofread and several quality control checkpoints are placed along the pathway. Here, we analyzed the fate of small nuclear RNAs (snRNAs) that are unable to acquire a ring of Sm proteins. We showed that snRNAs lacking the Sm ring are unstable and accumulate in P-bodies in an LSm1-dependent manner. We further provide evidence that defective snRNAs without the Sm binding site are uridylated at the 3' end and associate with DIS3L2 3'→5' exoribonuclease and LSm proteins. Finally, inhibition of 5'→3' exoribonuclease XRN1 increases association of ΔSm snRNAs with DIS3L2, which indicates competition and compensation between these two degradation enzymes. Together, we provide evidence that defective snRNAs without the Sm ring are uridylated and degraded by alternative pathways involving either DIS3L2 or LSm proteins and XRN1.

Indexed as

Nucleic Acid ConformationRNA TransportBase SequenceBinding SitesExoribonucleasesHeLa CellsHumansOrganellesProtein BindingProto-Oncogene ProteinsRNA-Binding ProteinsRNA, Small NuclearRNA StabilitySMN Complex ProteinsDIS3L2 protein, humanExoribonucleasesGEMIN5 protein, humanLSM1 protein, humanProto-Oncogene ProteinsRNA-Binding ProteinsRNA, Small NuclearSMN Complex Proteins

Identifiers

PMID32374871
PMCPMC7293007
OpenAlexW3021629576

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.